| IED ID | IndEnz0004000115 |
| Enzyme Type ID | xylanase000115 |
| Protein Name |
Endo-1,4-beta-xylanase 4 Xylanase 4 EC 3.2.1.8 1,4-beta-D-xylan xylanohydrolase 4 |
| Gene Name | XYL4 |
| Organism | Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Magnaporthales Pyriculariaceae Pyricularia Magnaporthe grisea (Crabgrass-specific blast fungus) (Pyricularia grisea) |
| Enzyme Sequence | MVSFTTILVAATAALVAANPVPPSIDEMREIYVKSRDLHARGGTPSSTGTHDGFYYSWWTDNGAQATYTNNAGGSYSITWSGNGNLVGGKGWNPGSARNVTYSANYRPNGNSYLSVYGWTRNPLVEYYVVENFGTYDPSSQASRKGTINVDGATYQVAQSTRTNQPSIDGTRTFQQYWSVRQQKRSSGTVDMKKHFDAWASMGMKLGTHDYQIVATEGYFSSGSSTVTIQR |
| Enzyme Length | 231 |
| Uniprot Accession Number | Q92245 |
| Absorption | |
| Active Site | ACT_SITE 126; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10062; ACT_SITE 217; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10063 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; |
| DNA Binding | |
| EC Number | 3.2.1.8 |
| Enzyme Function | FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; xylan degradation. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (1); Signal peptide (1) |
| Keywords | Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Secreted;Signal;Xylan degradation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,305 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |